Jacek Biesiadka

TL;DR: The most complete cyanobacterial photosystem II structure obtained so far is described, showing locations of and interactions between 20 protein subunits and 77 cofactors per monomer, and provides information about the Mn4Ca cluster, where oxidation of water takes place.

TL;DR: Polarized extended x-ray absorption fine structure measurements on PSII single crystals constrain the Mn4Ca cluster geometry to a set of three similar high-resolution structures, unlike either the 3.0 or 3.5 angstrom–resolution x-rays or other previously proposed models.

TL;DR: This case study shows that a careful evaluation of the structural intactness of the active site(s) by spectroscopic techniques can validate structures derived from crystallography and that it can be a valuable complementary method before structure-function correlations of metalloproteins can be made on the basis of high-resolution x-ray crystal structures.

TL;DR: In this article, the crystal structure of photosystem II (PSII) from the cyanobacterium Thermosynechococcus elongatus at 3.2 A resolution is presented.

TL;DR: It is suggested that titratable residues on the lumenal side of D1/D2 and PsbO form a polar channel, which might serve as a proton exit pathway associated with water oxidation on the Mn-cluster in an exergonic process out of PSII.